Monomer-monomer interactions drive the prepore to pore conversion of a beta-barrel-forming cholesterol-dependent cytolysin.

@article{Hotze2002MonomermonomerID,
  title={Monomer-monomer interactions drive the prepore to pore conversion of a beta-barrel-forming cholesterol-dependent cytolysin.},
  author={Eileen M. Hotze and Alejandro P Heuck and Daniel Mark Czajkowsky and Zhifeng Shao and Arthur E. Johnson and Rodney K. Tweten},
  journal={The Journal of biological chemistry},
  year={2002},
  volume={277 13},
  pages={11597-605}
}
Perfringolysin O (PFO), a cholesterol-dependent cytolysin, forms large oligomeric pore complexes comprised of up to 50 PFO molecules. In the present studies a mutant of PFO (PFO(Y181A)) has been identified that traps PFO in a multimeric prepore complex that cannot insert its transmembrane beta-hairpins and therefore cannot form a pore. Remarkably, PFO(Y181A) can be induced to insert its transmembrane beta-hairpins if functional PFO is incorporated into the PFO(Y181A) oligomeric prepore complex… CONTINUE READING

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